Structure and function of complex I in animals and plantsￂ -ￂ a comparative view
The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000kDa and includes 40-50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms..
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2017 |
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| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:161 |
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| Enthalten in: |
Physiologia plantarum - 161(2017), 1, Seite 6 |
| Sprache: |
Französisch |
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| Beteiligte Personen: |
Jennifer Senkler [VerfasserIn] |
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| Links: |
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| RVK: |
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| doi: |
10.1111/ppl.12561 |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Structure and function of complex I in animals and plantsￂ -ￂ a comparative view |
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| 520 | |a The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000kDa and includes 40-50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms. | ||
| 650 | 4 | |a Flowering | |
| 650 | 4 | |a Animals | |
| 650 | 4 | |a Atomic structure | |
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| 650 | 4 | |a Position (location) | |
| 650 | 4 | |a Kinases | |
| 650 | 4 | |a Plants (organisms) | |
| 650 | 4 | |a NADH dehydrogenase | |
| 650 | 4 | |a Homology | |
| 650 | 4 | |a Structure-function relationships | |
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| 650 | 4 | |a Electron transport chain | |
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| 700 | 0 | |a Hans-Peter Braun |4 oth | |
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